The feasibility of spectral editing techniques making use of heteronuclear scalar couplings in solid-state CPMAS NMR is demonstrated for powder samples exhibiting line widths of several tens of hertz such as ordinary amino acids. These simple and robust experiments are insensitive to molecular motion, they work at high MAS spinning rates, and yield unambiguous identification of carbon types in natural abundance samples in a manner directly analogous to liquid-state NMR. Examples are given for some amino acids and for cholesteryl acetate.